P67870 (CSK2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Casein kinase II subunit beta
Short name=CK II beta

Alternative name(s):
Phosvitin
Protein G5a

Gene names

Name:	CSNK2B
Synonyms:	CK2N, G5A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	215 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Participates in Wnt signaling By similarity. Plays a complex role in regulating the basal catalytic activity of the alpha subunit. Ref.16 Ref.19
Subunit structure	Tetramer composed of an alpha subunit, an alpha' subunit and two beta subunits. The beta subunit dimerization is mediated by zinc ions. Interacts with TCTEX1D3 By similarity. Interacts with CD163. Also component of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, the complex associating following UV irradiation. Interacts with MUSK; mediates phosphorylation of MUSK by CK2. Interacts with FGF1; this interaction is increased in the presence of FIBP, suggesting a possible cooperative interaction between CSNKB and FIBP in binding to FGF1. Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.27 Ref.28
Post-translational modification	Phosphorylated by alpha subunit. Ref.14 Ref.28
Sequence similarities	Belongs to the casein kinase 2 subunit beta family.
Sequence caution	The sequence CAI18393.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Wnt signaling pathway
Ligand	Metal-binding Zinc
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW adiponectin-activated signaling pathway Inferred from direct assay PubMed 19233263. Source: BHF-UCL axon guidance Traceable author statement. Source: Reactome cellular protein complex assembly Non-traceable author statement PubMed 19324893. Source: BHF-UCL endothelial tube morphogenesis Inferred from mutant phenotype PubMed 19592636. Source: BHF-UCL mitotic cell cycle Traceable author statement. Source: Reactome negative regulation of blood vessel endothelial cell migration Inferred from direct assay PubMed 19592636. Source: BHF-UCL negative regulation of cell proliferation Traceable author statement PubMed 19324893. Source: BHF-UCL positive regulation of activin receptor signaling pathway Inferred from mutant phenotype PubMed 19592636. Source: BHF-UCL positive regulation of pathway-restricted SMAD protein phosphorylation Inferred from direct assay PubMed 19592636. Source: BHF-UCL protein phosphorylation Traceable author statement Ref.4. Source: GOC regulation of DNA binding Non-traceable author statement PubMed 19324893. Source: BHF-UCL regulation of protein kinase activity Non-traceable author statement Ref.1. Source: GOC signal transduction Traceable author statement Ref.3. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay PubMed 19233263. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome extracellular vesicular exosome Inferred from direct assay PubMed 20458337. Source: UniProt nucleus Inferred from direct assay PubMed 21282530. Source: UniProtKB protein kinase CK2 complex Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	identical protein binding Inferred from physical interaction PubMed 10094392PubMed 14667819PubMed 21282530PubMed 21988832PubMed 23555304. Source: IntAct metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction PubMed 10094392Ref.28PubMed 12769847PubMed 14667819PubMed 16977309PubMed 19011756PubMed 20664522PubMed 21078624PubMed 21282530PubMed 21968188PubMed 21988832PubMed 23455922PubMed 23555304. Source: IntAct protein domain specific binding Inferred from physical interaction PubMed 11984006. Source: UniProtKB protein kinase regulator activity Non-traceable author statement Ref.1. Source: UniProtKB receptor binding Inferred from physical interaction PubMed 19233263PubMed 19592636. Source: BHF-UCL transcription factor binding Inferred from physical interaction PubMed 19324893. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		7	EBI-348169,EBI-348169
CACNA1A	O00555	2	EBI-348169,EBI-766279
CBX4	O00257-3	2	EBI-348169,EBI-4392727
Clip1	Q9JK25	2	EBI-348169,EBI-908338	From a different organism.
Clock	O08785	2	EBI-348169,EBI-79859	From a different organism.
CSNK2A1	P68400	13	EBI-348169,EBI-347804
CSNK2A2	P19784	6	EBI-348169,EBI-347451
PACS1	Q6VY07	3	EBI-348169,EBI-2555014
SIRT1	Q96EB6	5	EBI-348169,EBI-1802965

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 215

214

Casein kinase II subunit beta

PRO_0000068236

Regions

Region

188 – 193

6

Interaction with alpha subunit By similarity

Compositional bias

55 – 64

10

Asp/Glu-rich (acidic)

Sites

Metal binding

109

1

Zinc

Metal binding

114

1

Zinc

Metal binding

137

1

Zinc

Metal binding

140

1

Zinc

Amino acid modifications

Modified residue

2

1

N-acetylserine

Modified residue

2

1

Phosphoserine; by autocatalysis Ref.28

Modified residue

3

1

Phosphoserine; by autocatalysis Ref.28

Modified residue

209

1

Phosphoserine Ref.20 Ref.22 Ref.24 Ref.26

Modified residue

212

1

N6-acetyllysine Ref.23

Experimental info

Sequence conflict

194

1

P → A in AAA52123. Ref.3

Secondary structure

1

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215

Helix Strand Turn

Details...

Helix

9 – 15

7

Turn

17 – 20

4

Helix

27 – 31

5

Helix

33 – 36

4

Helix

39 – 41

3

Beta strand

43 – 45

3

Helix

46 – 53

8

Beta strand

59 – 61

3

Helix

67 – 87

21

Helix

91 – 102

12

Turn

103 – 106

4

Helix

112 – 114

3

Beta strand

120 – 122

3

Beta strand

134 – 136

3

Turn

138 – 140

3

Beta strand

142 – 144

3

Helix

149 – 151

3

Beta strand

152 – 155

4

Helix

156 – 158

3

Turn

159 – 162

4

Helix

163 – 170

8

Helix

172 – 174

3

Beta strand

187 – 189

3

Beta strand

190 – 192

3

Helix

195 – 198

4

Turn

199 – 201

3

Helix

202 – 205

4

Sequences

	Sequence		Length	Mass (Da)
	P67870 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: E465B1E699B0E0EC	FASTA	215	24,942
	10 20 30 40 50 60 MSSSEEVSWI SWFCGLRGNE FFCEVDEDYI QDKFNLTGLN EQVPHYRQAL DMILDLEPDE 70 80 90 100 110 120 ELEDNPNQSD LIEQAAEMLY GLIHARYILT NRGIAQMLEK YQQGDFGYCP RVYCENQPML 130 140 150 160 170 180 PIGLSDIPGE AMVKLYCPKC MDVYTPKSSR HHHTDGAYFG TGFPHMLFMV HPEYRPKRPA 190 200 210 NQFVPRLYGF KIHPMAYQLQ LQAASNFKSP VKTIR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human phosvitin/casein kinase type II. Molecular cloning and sequencing of full-length cDNA encoding subunit beta." Jakobi R., Voss H., Pyerin W. Eur. J. Biochem. 183:227-233(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Expression of the cDNA for the beta subunit of human casein kinase II confers partial UV resistance on xeroderma pigmentosum cells." Teitz T., Eli D., Penner M., Bakhanashvili M., Naiman T., Timme T.L., Wood C.M., Moses R.E., Canaani D. Mutat. Res. 236:85-97(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Cloning and characterization of a cDNA encoding the beta subunit of human casein kinase II." Heller-Harrison R.A., Meisner H., Czech M.P. Biochemistry 28:9053-9058(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Structure of the gene encoding human casein kinase II subunit beta." Voss A., Wirkner U., Jacobi R., Hewitt N., Schwager C., Zimmermann J., Ansorge W., Pyerin W. J. Biol. Chem. 266:13706-13711(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Sequencing of full-length cDNA encoding the alpha and beta subunits of human casein kinase II from human platelets and megakaryocytic cells. Expression of the casein kinase IIalpha intronless gene in a megakaryocytic cell line." Singh L.S., Kalafatis M. Biochemistry 41:8935-8940(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse." Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L. Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region." Shiina S., Tamiya G., Oka A., Inoko H. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[10]	NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[11]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[14]	"Stimulation of casein kinase II by epidermal growth factor: relationship between the physiological activity of the kinase and the phosphorylation state of its beta subunit." Ackerman P., Glover C.V., Osheroff N. Proc. Natl. Acad. Sci. U.S.A. 87:821-825(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[15]	"Interaction of CD163 with the regulatory subunit of casein kinase II (CKII) and dependence of CD163 signaling on CKII and protein kinase C." Ritter M., Buechler C., Kapinsky M., Schmitz G. Eur. J. Immunol. 31:999-1009(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CD163.
[16]	"A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1." Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H., Goodman R., Lozano G., Zhao Y., Lu H. Mol. Cell 7:283-292(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SSRP1 AND SUPT16H.
[17]	"Identification of ribosome-binding protein p34 as an intracellular protein that binds acidic fibroblast growth factor." Skjerpen C.S., Wesche J., Olsnes S. J. Biol. Chem. 277:23864-23871(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FGF1.
[18]	"p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex." Keller D.M., Lu H. J. Biol. Chem. 277:50206-50213(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SSRP1 AND SUPT16H.
[19]	"Casein kinase 2-dependent serine phosphorylation of MuSK regulates acetylcholine receptor aggregation at the neuromuscular junction." Cheusova T., Khan M.A., Schubert S.W., Gavin A.C., Buchou T., Jacob G., Sticht H., Allende J., Boldyreff B., Brenner H.R., Hashemolhosseini S. Genes Dev. 20:1800-1816(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MUSK, INTERACTION WITH MUSK.
[20]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[21]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[22]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[25]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]	"Crystal structure of the human protein kinase CK2 regulatory subunit reveals its zinc finger-mediated dimerization." Chantalat L., Leroy D., Filhol O., Nueda A., Benitez M.J., Chambaz E.M., Cochet C., Dideberg O. EMBO J. 18:2930-2940(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 1-182, SUBUNIT, ZINC-BINDING SITES.
[28]	"Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme." Niefind K., Guerra B., Ermakowa I., Issinger O.G. EMBO J. 20:5320-5331(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CSNK2A1, ZINC-BINDING SITES, SUBUNIT, PHOSPHORYLATION AT SER-2 AND SER-3.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X16937 mRNA. Translation: CAA34811.1.
X16312 mRNA. Translation: CAA34379.1.
M30448 mRNA. Translation: AAA52123.1.
X57152 Genomic DNA. Translation: CAA40442.1.
AY113186 mRNA. Translation: AAM50092.1.
CR541699 mRNA. Translation: CAG46500.1.
AF129756 Genomic DNA. Translation: AAD18081.1.
BA000025 Genomic DNA. Translation: BAB63386.1.
DQ314868 Genomic DNA. Translation: ABC40727.1.
AK311860 mRNA. Translation: BAG34801.1.
AL662899 Genomic DNA. Translation: CAI96141.1.
AL662899 Genomic DNA. Translation: CAI18393.2. Different initiation.
AL670886 Genomic DNA. Translation: CAI17800.1.
AL805934 Genomic DNA. Translation: CAI18523.1.
BX511262 Genomic DNA. Translation: CAM45825.1.
CR753842 Genomic DNA. Translation: CAQ06572.1.
CR354443 Genomic DNA. Translation: CAQ07002.1.
CR759761 Genomic DNA. Translation: CAQ10879.1.
CH471081 Genomic DNA. Translation: EAX03473.1.
BC112017 mRNA. Translation: AAI12018.1.
BC112019 mRNA. Translation: AAI12020.1.

CCDS

CCDS4712.1.

PIR

A39459.

RefSeq

NP_001269314.1. NM_001282385.1.
NP_001311.3. NM_001320.6.

UniGene

Hs.73527.

3D structure databases

PDBe
RCSB-PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DS5	X-ray	3.16	E/F/G/H	181-203	[»]
1JWH	X-ray	3.10	C/D	1-215	[»]
1QF8	X-ray	1.74	A/B	1-182	[»]
3EED	X-ray	2.80	A/B	1-193	[»]
4DGL	X-ray	3.00	A/B	1-215	[»]
4MD7	X-ray	3.10	A/B/C/D	1-215	[»]
4MD8	X-ray	3.30	A/B/C/D	1-215	[»]
4MD9	X-ray	3.50	A/B/C/D/I/J/N/O	1-215	[»]
4NH1	X-ray	3.30	C/D	1-215	[»]

ProteinModelPortal

P67870.

SMR

P67870. Positions 7-207.

ModBase

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MobiDB

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Protein-protein interaction databases

BioGrid

107843. 212 interactions.

DIP

DIP-131N.

IntAct

P67870. 178 interactions.

MINT

MINT-88683.

STRING

9606.ENSP00000415615.

Chemistry

BindingDB

P67870.

ChEMBL

CHEMBL2358.

Polymorphism databases

DMDM

54037520.

Proteomic databases

MaxQB

P67870.

PaxDb

P67870.

PRIDE

P67870.

Protocols and materials databases

DNASU

1460.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000375865; ENSP00000365025; ENSG00000204435.
ENST00000375866; ENSP00000365026; ENSG00000204435.
ENST00000375882; ENSP00000365042; ENSG00000204435.
ENST00000383427; ENSP00000372919; ENSG00000206406.
ENST00000383433; ENSP00000372925; ENSG00000206406.
ENST00000400110; ENSP00000382980; ENSG00000206406.
ENST00000412802; ENSP00000413469; ENSG00000224774.
ENST00000418230; ENSP00000411322; ENSG00000228875.
ENST00000422567; ENSP00000407018; ENSG00000224398.
ENST00000429633; ENSP00000409510; ENSG00000230700.
ENST00000431476; ENSP00000394855; ENSG00000224398.
ENST00000436169; ENSP00000412520; ENSG00000224398.
ENST00000443673; ENSP00000400188; ENSG00000230700.
ENST00000448596; ENSP00000391038; ENSG00000232960.
ENST00000451917; ENSP00000415303; ENSG00000224774.
ENST00000452985; ENSP00000415237; ENSG00000228875.
ENST00000453234; ENSP00000395275; ENSG00000224774.
ENST00000454382; ENSP00000390900; ENSG00000232960.
ENST00000454511; ENSP00000393756; ENSG00000232960.
ENST00000455161; ENSP00000407379; ENSG00000230700.
ENST00000458330; ENSP00000410802; ENSG00000228875.

GeneID

1460.

KEGG

hsa:1460.

UCSC

uc003nvr.1. human.

Organism-specific databases

CTD

1460.

GeneCards

GC06P031633.
GC06Pj31620.
GC06Pk31615.
GC06Pl31672.
GC06Pm31709.
GC06Pn31623.
GC06Po31622.

HGNC

HGNC:2460. CSNK2B.

HPA

CAB004349.
CAB013087.
CAB016059.
HPA005944.

MIM

115441. gene.

neXtProt

NX_P67870.

PharmGKB

PA26960.

GenAtlas

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Phylogenomic databases

eggNOG

COG5041.

HOGENOM

HOG000039270.

HOVERGEN

HBG051131.

InParanoid

P67870.

KO

K03115.

PhylomeDB

P67870.

TreeFam

TF314462.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

SignaLink

P67870.

Gene expression databases

Bgee

P67870.

CleanEx

HS_CSNK2B.

Genevestigator

P67870.

Family and domain databases

Gene3D

1.10.1820.10. 1 hit.
2.20.25.20. 1 hit.

InterPro

IPR016149. Casein_kin_II_reg-sub_a-hlx.
IPR016150. Casein_kin_II_reg-sub_b-sht.
IPR000704. Casein_kinase_II_reg-sub.
[Graphical view]

PANTHER

PTHR11740. PTHR11740. 1 hit.

Pfam

PF01214. CK_II_beta. 1 hit.
[Graphical view]

PRINTS

PR00472. CASNKINASEII.

SMART

SM01085. CK_II_beta. 1 hit.
[Graphical view]

SUPFAM

SSF57798. SSF57798. 1 hit.

PROSITE

PS01101. CK2_BETA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P67870.

GeneWiki

CSNK2B.

GenomeRNAi

1460.

NextBio

6001.

PRO

P67870.

SOURCE

Search...

Entry information

Entry name

CSK2B_HUMAN

Accession

Primary (citable) accession number: P67870
Secondary accession number(s): B0UXA9 , P07312, P13862, Q4VX47

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	July 9, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.